Nuclear magnetic resonance structural patterns

One has seen that the number of individual components in a hydrocarbon cut increases rapidly with its boiling point. It is thereby out of the question to resolve such a cut to its individual components instead of the analysis by family given by mass spectrometry, one may prefer a distribution by type of carbon. This can be done by infrared absorption spectrometry which also has other applications in the petroleum industry. Another distribution is possible which describes a cut in tei ns of a set of structural patterns using nuclear magnetic resonance of hydrogen (or carbon) this can thus describe the average molecule in the fraction under study. 

The structures of vanicosides A (1) and B (2) and hydropiperoside (3) were established primarily by one- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy techniques and fast atom bombardment (FAB) mass spectrometry (MS).22 The presence of two different types of phenylpropanoid esters in 1 and 2 was established first through the proton (4H) NMR spectra which showed resonances for two different aromatic substitution patterns in the spectrum of each compound. Integration of the aromatic region defined these as three symmetrically substituted phenyl rings, due to three p-coumaryl moieties, and one 1,3,4-trisubstituted phenyl ring, due to a feruloyl ester. The presence of a sucrose backbone was established by two series of coupled protons between 3.2 and 5.7 ppm in the HNMR spectra, particularly the characteristic C-l (anomeric) and C-3 proton doublets... 

Protein structure The three-dimensional structure of a protein can be determined almost to the determination atomic level by the techniques of X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. In X-ray crystallography a crystal of the protein to be visualized is exposed to a beam of X-rays and the resulting diffraction pattern caused as the X-rays encounter the protein crystal is recorded on photographic film. The intensities of the diffraction maxima (the darkness of the spots on the film) are then used to mathematically construct the three-dimensional image of the protein crystal. NMR spectroscopy can be used to determine the three-dimensional structures of small (up to approximately 30 kDa) proteins in aqueous solution. 

Nuclear Magnetic Resonance Spectroscopy. Nmr is a most valuable technique for structure determination in thiophene chemistry, especially because spectral interpretation is much easier in the thiophene series compared to benzene derivatives. Chemical shifts in proton nmr are well documented for thiophene (CDC13), 6 = H2 7.12, H3 7.34, H4 7.34, and H5 7.12 ppm. Coupling constants occur in well-defined ranges J2 3 = 4.9-5.8 J3 4 = 3.45-4.35 J2 4 = 1.25-1.7 and J2 5 = 3.2-3.65 Hz. The technique can be used quantitatively by comparison with standard spectra of materials of known purity. 13C-nmr spectroscopy of thiophene and thiophene derivatives is also a valuable technique that shows well-defined patterns of spectra. 13C chemical shifts for thiophene, from tetramethylsilane (TMS), are C2 127.6, C3 125.9, C4 125.9, and C5 127.6 ppm. 

In fact, a tremendous amount of information is available on the structures of biological macromolecules descriptions of structures of proteins and nucleic acids make up major portions of modern textbooks in biochemistry and molecular biology. The Protein Data Bank and the Nucleic Acid Database are online archives that contain sequence and structural data on thousands of specific molecules and complexes of molecules. This structural information comes from in vitro experiments, with structures inferred from the x-ray diffraction patterns of crystallized molecules, spectroscopic measurements using multi-dimensional nuclear magnetic resonance, and a host of other methodologies. 

X-Ray structural determinations and nuclear magnetic resonance (NMR) studies have become versatile tools in the elucidation of the structure of the five-membered metallacycles. Structural and NMR patterns are comprehensively outlined in CHEC-II(1996) <1996CHEC-II(2)933>. Herein we occasionally refer when necessary to the results of structural studies in the reactivity and synthetic sections. 

Structural characterization by nuclear magnetic resonance (NMR) methods is routine and, in general, mention of the results has been deferred to the sections dealing with the synthesis of particular heterocycles. This section includes results where sufficient work has been performed to suggest patterns and where more unusual techniques have been discussed. 

Of all the methods available for the physical characterization of solid materials, it is generally agreed that crystallography, microscopy, thermal analysis, solubility studies, vibrational spectroscopy, and nuclear magnetic resonance are the most useful for characterization of polymorphs and solvates. However, it cannot be overemphasized that the defining criterion for the existence of polymorphic types must always be a non-equivalence of crystal structures. For compounds of pharmaceutical interest, this ordinarily implies that a non-equivalent X-ray powder diffraction pattern is observed for each suspected polymorphic variation. All other methodologies must be considered as sources of supporting and ancillary information, but cannot be taken as definitive proof for the existence of polymorphism by themselves. 

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